Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P0C0V0 | DEGP_ECOLI | MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVL... | 3.4.21.107 | null | chaperone-mediated protein folding [GO:0061077]; positive regulation of apoptotic process [GO:0043065]; programmed cell death [GO:0012501]; protein folding [GO:0006457]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; proteolysis [GO:0006508]; response to heat [GO:0009408]; resp... | outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00595;PF13365; | 2.30.42.10;2.40.10.120; | Peptidase S1C family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9083020}; Peripheral membrane protein {ECO:0000269|PubMed:9083020}; Cytoplasmic side {ECO:0000269|PubMed:9083020}. | CATALYTIC ACTIVITY: Reaction=Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107; Evidence={ECO:0000269|PubMed:8830688}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 55 degrees Celsius. In the range from 37 to 55 degrees Celsius, the proteolytic activity rapidly increases with temperature. {ECO:0000269|PubMed:7744744}; | FUNCTION: DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures (PubMed:10319814). Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867). DegP is... | Escherichia coli (strain K12) |
P0C0V8 | RS21A_YEAST | MENDKGQLVELYVPRKCSATNRIIKADDHASVQINVAKVDEEGRAIPGEYVTYALSGYVRSRGESDDSLNRLAQNDGLLKNVWSYSR | null | null | endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000461]; translation [GO:0006412] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | structural constituent of ribosome [GO:0003735] | PF01249; | 3.30.1230.20; | Eukaryotic ribosomal protein eS21 family | PTM: N-terminally acetylated by acetyltransferase NatB. {ECO:0000269|PubMed:10601260}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14627813, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C0V9 | HEMA_BRV1 | MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTV... | 3.1.1.53 | null | fusion of virus membrane with host plasma membrane [GO:0019064] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | carbohydrate binding [GO:0030246]; host cell surface receptor binding [GO:0046789]; sialate 4-O-acetylesterase activity [GO:0106331]; sialate 9-O-acetylesterase activity [GO:0106330]; sialate O-acetylesterase activity [GO:0001681] | PF03996;PF02710; | null | Influenza type C/coronaviruses hemagglutinin-esterase family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis... | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; Evidence={ECO:0000269|PubMed:19721004}; CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-... | null | null | null | null | FUNCTION: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and suscep... | Breda virus 1 (BRV-1) |
P0C0W9 | RL11A_YEAST | MSAKAQNPMRDLKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRDRNFSATGNFGFGIDEHIDLGIKYDPSIGIFGMDFYVVMNRPGARVTRRKRCKGTVGNSHKTTKEDTVSWFKQKYDADVLDK | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027]; translation [GO:0006412] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; nucleus [GO:0005634] | RNA binding [GO:0003723]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00281;PF00673; | 3.30.1440.10; | Universal ribosomal protein uL5 family | PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 complex is transported into the nucleus by KAP104. {ECO:0000269|PubMed:23118189}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C0X0 | RS28B_YEAST | MDSKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDTSRTIVRNVKGPVRENDILVLMESEREARRLR | null | null | cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA [GO:0030490]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; ribosomal small subunit assembly [GO:0000028]; ribosomal subunit export from nucleus [GO:0000054] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | structural constituent of ribosome [GO:0003735] | PF01200; | 2.40.50.140; | Eukaryotic ribosomal protein eS28 family | PTM: N-terminally acetylated by acetyltransferase NatB. {ECO:0000269|PubMed:10601260}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C0Y5 | NMTDH_DAVTA | MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAARGCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKCQVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDGSVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITASMSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVNSISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKGAYVYFASDASTYTTGADLLIDGGYTTR | 1.1.1.138 | null | mannitol metabolic process [GO:0019594]; protein homotetramerization [GO:0051289] | null | mannitol 2-dehydrogenase (NADP+) activity [GO:0050085]; NADP binding [GO:0050661]; oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor [GO:0050664]; protein homodimerization activity [GO:0042803] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | null | CATALYTIC ACTIVITY: Reaction=D-mannitol + NADP(+) = D-fructose + H(+) + NADPH; Xref=Rhea:RHEA:16765, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899, ChEBI:CHEBI:37721, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.138; Evidence={ECO:0000269|PubMed:16608840}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16766; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.17 uM for D-fructose (at pH 7.5) {ECO:0000269|PubMed:16608840}; KM=0.23 uM for D-mannitol (at pH 7.5) {ECO:0000269|PubMed:16608840}; KM=53 uM for NADPH (at pH 7.5) {ECO:0000269|PubMed:16608840}; KM=67 uM for NADP(+) (at pH 7.5) {ECO:0000269|PubMed:16608840}; | null | null | null | FUNCTION: Interconverts D-mannitol and D-fructose. Not active with fructose 6-phosphate or NADH. {ECO:0000269|PubMed:16608840}. | Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum) |
P0C0Z7 | CH60_CHLTR | MVAKNIKYNEEARKKIQKGVKTLAEAVKVTLGPKGRHVVIDKSFGSPQVTKDGVTVAKEVELADKHENMGAQMVKEVASKTADKAGDGTTTATVLAEAIYTEGLRNVTAGANPMDLKRGIDKAVKVVVDQIRKISKPVQHHKEIAQVATISANNDAEIGNLIAEAMEKVGKNGSITVEEAKGFETVLDIVEGMNFNRGYLSSYFATNPETQECVLEDALVLIYDKKISGIKDFLPVLQQVAESGRPLLIIAEDIEGEALATLVVNRIRGGFRVCAVKAPGFGDRRKAMLEDIAILTGGQLISEELGMKLENANLAMLGKA... | 5.6.1.7 | null | chaperone cofactor-dependent protein refolding [GO:0051085]; mitochondrial unfolded protein response [GO:0034514]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of T cell activation [GO:0050870]; positive regulation of ... | GroEL-GroES complex [GO:1990220] | ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; isomerase activity [GO:0016853]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | Chaperonin (HSP60) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00600}; | null | null | null | null | FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:... | Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx) |
P0C152 | MKS3_RAT | MVMRTRPLAAMAVRSCFSALTGTVYLLLVLCEVSWAQIFSFPFQRPETCDLNQYFDISALSCAPCGANQRRDALGTSCICLPGYHMISNNGGPSIICKKCPENMKGVTKDGWDCISCPNGLTAEGKCHCPSGHILVERNVSGSLLSQATCELCDGNENSFTKPNALGTRCVRCEPTFVNTSRSCSCSEPHISTGGLCFSNTGNFPQRLISTERYGELGMSSNSEWFTKYLQATAAACWTHSNLTSCQALGNMCVMNMNSYDSTTFDACRLFHYVFEGAAGLTGVHSVPFWRQNLPWLFYGDQPGLASQVLSTTPLPTNFS... | null | null | branching morphogenesis of an epithelial tube [GO:0048754]; cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; head development [GO:0060322]; heart development [GO:0007507]; kidney development [GO:0001822]; negative reg... | centrosome [GO:0005813]; ciliary membrane [GO:0060170]; ciliary transition zone [GO:0035869]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; MKS complex [GO:0036038] | filamin binding [GO:0031005]; misfolded protein binding [GO:0051787]; unfolded protein binding [GO:0051082] | PF09773; | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5HYA8}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19815549}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5HYA8}. Note=Localizes at the transit... | null | null | null | null | null | FUNCTION: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appr... | Rattus norvegicus (Rat) |
P0C169 | H2A1C_RAT | MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Rattus norvegicus (Rat) |
P0C170 | H2A1E_RAT | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Rattus norvegicus (Rat) |
P0C191 | GPVI_MOUSE | MSPASPTFFCIGLCVLQVIQTQSGPLPKPSLQAQPSSLVPLGQSVILRCQGPPDVDLYRLEKLKPEKYEDQDFLFIPTMERSNAGRYRCSYQNGSHWSLPSDQLELIATGVYAKPSLSAHPSSAVPQGRDVTLKCQSPYSFDEFVLYKEGDTGSYKRPEKWYRANFPIITVTAAHSGTYRCYSFSSSSPYLWSAPSDPLVLVVTGLSATPSQVPTEESFPVTESSRRPSILPTNKISTTEKPMNITASPEGLSPPFGFAHQHYAKGNLVRICLGATIIIILLGLLAEDWHSRKKCLQHRMRALQRPLPPLPLA | null | null | collagen-activated signaling pathway [GO:0038065]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; platelet aggregation [GO:0070527] | cell surface [GO:0009986]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197] | collagen binding [GO:0005518]; collagen receptor activity [GO:0038064]; protein tyrosine kinase binding [GO:1990782] | PF13895; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24368846}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Collagen receptor involved in collagen-induced platelet adhesion and activation (PubMed:16139873, PubMed:24368846). Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signalin... | Mus musculus (Mouse) |
P0C192 | LRC4B_MOUSE | MAQAHIRGSPCPLLPPGRMSWPHGALLLLWLFSPPLRAGGGGVAVTSAAGGGSPPATSCPAACSCSNQASRVICTRRELAEVPASIPVNTRYLNLQENSIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCD... | null | null | positive regulation of synapse assembly [GO:0051965]; regulation of postsynaptic density assembly [GO:0099151]; regulation of presynapse assembly [GO:1905606]; synaptic membrane adhesion [GO:0099560] | cerebellar mossy fiber [GO:0044300]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734] | signaling receptor binding [GO:0005102] | PF07679;PF00560;PF13855; | 2.60.40.10;3.80.10.10; | null | PTM: N-glycosylated. O-glycosylated; contains sialic acid. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Presynaptic cell membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P0C195 | CM3A_CONKI | KRNGCCNCSSKWCRDHSRCCGR | null | null | null | extracellular region [GO:0005576] | sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | null | null | Conotoxin M superfamily | PTM: Toxins with three different disulfide connectivities have been synthesized (PubMed:23167564, PubMed:35167877). The conotoxin mu-KIIIA-P1 shows the connectivity C1-C5, C2-C4, and C3-C6, whereas mu-KIIIA-P2 shows the connectivity C1-C6, C2-C4, and C3-C5 (PubMed:23167564). The conotoxin mu-KIIIA-N has the 'native' fo... | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15882064}. | null | null | null | null | null | FUNCTION: Mu-conotoxin KIIIA-P1: mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks Nav1.2/SCN2A (IC(50)5-124 nM), Nav1.4/SCN4A (IC(50)=20-90 nM), and Nav1.7/SCN9A (IC(50)=290-413 nM) (PubMed:17724025, PubMed:19221510, PubMed:21652775, PubMed:21709136, PubMed:21781281, PubMed:23146020, ... | Conus kinoshitai (Kinoshita's cone) |
P0C1A7 | PLYL_DICD3 | MKYLNCFISTGLAAFFLVNSTSVLAADCSSDLTSGISTKRIYYVAPNGNSSNNGSSFNAPMSFSAAMAAVNPGELILLKPGTYTIPYTQGKGNTITFNKSGKDGAPIYVAAANCGRAVFDFSFPDSQWVQASYGFYVTGDYWYFKGVEVTRAGYQGAYVIGSHNTFENTAFHHNRNTGLEINNGGSYNTVINSDAYRNYDPKKNGSMADGFGPKQKQGPGNRFVGCRAWENSDDGFDLFDSPQKVVIENSWAFRNGINYWNDSAFAGNGNGFKLGGNQAVGNHRITRSVAFGNVSKGFDQNNNAGGVTVINNTSYKNGIN... | 4.2.2.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8577252}; | pectin catabolic process [GO:0045490]; symbiont-mediated disruption of host cell wall [GO:0052009] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; pectate lyase activity [GO:0030570] | PF13229; | 2.160.20.10; | Polysaccharide lyase 9 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.2; Evidence={ECO:0000269|PubMed:10368144, ECO:0000269|PubMed:8577252}; | null | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 8.0. {ECO:0000269|PubMed:8577252}; | null | FUNCTION: Presents an endo-cleaving activity on polygalacturonate or partially methylated pectin. Is effective in the maceration of plant tissue, and has an important role in soft-rot disease. Is 280-fold less active against polygalacturonate than the major pectate lyase PelB. When assayed on polygalacturonate, PelL re... | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) |
P0C1A9 | PMEA_DICD3 | MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNP... | 3.1.1.11 | null | cell wall modification [GO:0042545]; pectin catabolic process [GO:0045490] | cell outer membrane [GO:0009279]; extracellular space [GO:0005615] | aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599] | PF01095; | 2.160.20.10; | Pectinesterase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8370537}. Note=Upon overexpression also accumulates in the periplasm. {ECO:0000269|PubMed:8370537}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;... | null | PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. {ECO:0000305|PubMed:17717531, ECO:0000305|PubMed:8370537}. | null | null | FUNCTION: Catalyzes the first step in maceration and soft-rotting of plant tissue. {ECO:0000305|PubMed:17717531, ECO:0000305|PubMed:8370537}. | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) |
P0C1B3 | AMYA1_ASPOR | MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNP... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074}; Note=Binds 2 calcium ions per subunit (PubMed:16880540, PubMed:6609921, PubMed:9283074). Calcium is inhibitory at high concentrations. {ECO:0000269|PubMed:16880540, ECO:0000269|... | carbohydrate catabolic process [GO:0016052] | cell septum [GO:0030428]; cell wall-bounded periplasmic space [GO:0030287]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal septin band [GO:0032163]; spitzenkorper [GO:0031521] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509] | PF09260;PF00128; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000305}; | null | null | null | null | null | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
P0C1D0 | CA1A_CONRE | SNKRKNAAMLDMIAQHAIRGCCSDPRCRYRCR | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Conotoxin A superfamily | PTM: The disulfide bond CysI-CysIII is important for alpha-9-alpha-10 subtype inhibition, whereas the bond CysII-CysIV contributes to GABA(B) modulation. {ECO:0000269|PubMed:25393758}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: This toxin target two types of receptors, the nicotinic acetylcholine receptor (nAChR) and the G-protein-coupled receptor GABA(B). It specifically inhibits the alpha-9-alpha-10/CHRNA9-CHRNA10 nAChR, with preference for rat receptors (PubMed:16445293, PubMed:18242183, PubMed:18295795, PubMed:21888386, PubMed:2... | Conus regius (Crown cone) |
P0C1G9 | SOX11_RAT | MVQQAESSEAESNLPRDALDTEEGEFMACSPVALDESDPDWCKTASGHIKRPMNAFMVWSKIERRKIMEQSPDMHNAEISKRLGKRWKMLKDSEKIPFIREAERLRLKHMADYPDYKYRPRKKPKTDPAAKPSAGQSPDKSAAGAKAAKGPGKKCAKLKAPAGKAGAGKAAQPGDCGAGKAAKCVFLDDDDEEDDEDDELQLRPKPDADDDDDEPAHSHLLPPPAQQQPPQLLRRYSVAKVPASPTLSSAAESPEGASLYDEVRAGGRLYYSFKNITKQQPPPAPPALSPASSRCVSTSSSSGSSSGSGAEDADDLMFDL... | null | null | brain development [GO:0007420]; camera-type eye morphogenesis [GO:0048593]; closure of optic fissure [GO:0061386]; cornea development in camera-type eye [GO:0061303]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic skeletal system morphogenesis [GO:0048704]; eyelid development in camera-type eye [GO:006... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; t... | PF00505; | 1.10.30.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7M6Y2, ECO:0000255|PROSITE-ProRule:PRU00267}. | null | null | null | null | null | FUNCTION: Transcription factor that acts as a transcriptional activator (By similarity). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By sim... | Rattus norvegicus (Rat) |
P0C1H3 | H2B1_CHICK | MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | null | null | defense response to bacterium [GO:0042742] | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination of Lys-121 by the BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 during apoptosis; which facilitates apoptotic chromatin condensation. {EC... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Gallus gallus (Chicken) |
P0C1H4 | H2B5_CHICK | MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRRKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | null | null | null | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination of Lys-121 by the BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 during apoptosis; which facilitates apoptotic chromatin condensation. {EC... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Gallus gallus (Chicken) |
P0C1H5 | H2B7_CHICK | MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKRARKESYSIYVYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | null | null | null | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination of Lys-121 by the BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 during apoptosis; which facilitates apoptotic chromatin condensation. {EC... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Gallus gallus (Chicken) |
P0C1J9 | TAT_HV1MP | MEVVDPKIDPWNHPGSQPETPCNNCYCKKCCFHCPLCFMKKGLGISYGRKKRRQRRRTPQGSKIHQDPVPKQPLSQTRGDPTGPEESKKKVESQTETDP | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype F2 (isolate MP255) (HIV-1) |
P0C1K0 | TAT_HV1M2 | MEVVDPNLDPWKHPGSQPETPCNKCYCKKCCFHCQLCFTRKGLGISYGRKKRRQRRRTPQSGEVHQDPVSKQPLSQTRGDPKGPEESKKKVESKTKTDPSD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype F2 (isolate MP257) (HIV-1) |
P0C1K1 | TAT_HV1AN | MDPVDPEVPPWHHPGSQPQIPCNNCYCKRCCYHCYVCFVRKGLGISYGRKKRGRPAAASHPDHKDPVPKQSPTITKRKQERQEEQEEEVEKKAGPGGYPRRKGSCHCCTRTSEQ | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group O (isolate ANT70) (HIV-1) |
P0C1K2 | TAT_HV1MV | MDPVDPEMPPWHHPGSKPQTPCNNCYCKRCCYHCYVCFTKKGLGISHGRKKRRRPAAAASYPDNKDPVPEQHTGRKQKRQEEQEKKVEKETGPSGQPCHQDSCNSCTRISGQ | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group O (isolate MVP5180) (HIV-1) |
P0C1K3 | TAT_HV197 | MEPVDPNIEPWNQPGSQPKTACNQCYCKKCCYHCQLCFLQKGLGICYGREKRRQRTTTPYASKNHKDPIPKQPLPQARGDPTGPKESKKEVESKTKTDP | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype K (isolate 97ZR-EQTB11) (HIV-1) |
P0C1K4 | TAT_HV196 | MDPVDPNIEPWNQPGSQPKTACNQCYCKRCCYHCQICFLKKGLGISNGRKKRRPRRTTPYNSENHQDPLRKQPLSQPRGEQTDPKESKKKVESKTKTDQFD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype K (isolate 96CM-MP535) (HIV-1) |
P0C1K7 | GAG_HV19N | MGARASVLSGGKLDSWEKIRLRPGGRKKYKLKHIVWASRELGRFALNRDLLETAEGCVQIMKQLQPALTGTEELRSLFNTVATLYCVHQKIEVKDTKEAPEEVEKIQKNSQQEIQQAAKNEGNSNPVSQNYPIVQNAQGQMIHQAISPWTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINDEAAEWDRIHPQQAGPIPPGQIREPSGSDIAGTTSTLQEQIRWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKGWMTDTL... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype G (isolate 92NG083) (HIV-1) |
P0C1Q2 | PDE11_MOUSE | MAASRLDFGEVETFLDRHPELFEDYLMRKGKQELVDKWLQRHTSGQGASSLRPALAGASSLAQSNAKGSPGIGGGAGPQGSAHSHPTPGGGESAGVPLSPSWASGSRGDGSLQRRASQKELRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRVNLPQYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNDEIDKLTGYKT... | 3.1.4.35; 3.1.4.53 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:O76083}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250|UniProtKB:O76083}; | cAMP-mediated signaling [GO:0019933]; metabolic process [GO:0008152]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of cGMP-mediated signaling [GO:0010754] | cytosol [GO:0005829]; perikaryon [GO:0043204] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cGMP binding [GO:0030553]; cGMP-stimulated cyclic-nucleotide phosphodiesterase activity [GO:0004118]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; metal ion binding [GO:0046872] | PF01590;PF00233; | 3.30.450.40;1.10.1300.10; | Cyclic nucleotide phosphodiesterase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9HCR9}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000250|UniProtKB:Q9HCR9}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15... | null | null | null | null | FUNCTION: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP (PubMed:15800654). Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively (By similarity). {ECO:0000250|UniProtKB:Q9HCR9, ECO:0000269|PubMed:15800654}. | Mus musculus (Mouse) |
P0C1Q3 | PCAT2_RAT | MNRCAEAAAVAATVPGSGVGDSGLRPPMVPRQASFFPPPVPNPFVQQTRISAARRLQMILLGIILLPVRALLVGLVLLLAWPFAVISTVCCPKKLTHPISDWRRKITQPALKFLGRAMFFSMGFRVTVKGKVASPLEAPIFVVAPHSTFFDGIACVVAGLPSLVSRNENAQTPLVGRLLRALQPVLVSRVDPDSRKNTINEIKKRAMSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCVLTFCQLFTKVEVEFMPVQAPSEEERNDPVLFASRVRNLMAEALEIPVTD... | 2.3.1.23; 2.3.1.25; 2.3.1.51; 2.3.1.67 | null | membrane organization [GO:0061024]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; platelet activating factor biosynthetic process [GO:0006663] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; lipid droplet [GO:0005811]; membrane [GO:0016020]; plasma membrane [GO:0005886] | 1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; 1-alkenylglycerophosphocholine O-acyltransferase activity [GO:0047159]; 1-alkylglycerophosphocholine O-acetyltransferase activity [GO:0047192]; calcium ion binding [GO:0005509]; lysop... | PF01553;PF13499; | 1.10.238.10; | 1-acyl-sn-glycerol-3-phosphate acyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7L5N7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7L5N7}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8BYI6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7L5N7}. Cell membrane {ECO:0000250|UniProtKB:Q8B... | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000250|UniProtKB:Q7L5N7}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl... | null | PATHWAY: Lipid metabolism; phospholipid metabolism. | null | null | FUNCTION: Exhibits both acyltransferase and acetyltransferase activities (By similarity). Activity is calcium-dependent (By similarity). Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (By similarity)... | Rattus norvegicus (Rat) |
P0C1Q4 | MASTI_POLPI | IDWKKLLDAAKQIL | null | null | chemotaxis [GO:0006935]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; positive regulation of chemotaxis [GO:0050921] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | MCD family, Mastoparan subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16129513}. Target cell membrane {ECO:0000269|PubMed:18328599, ECO:0000269|PubMed:28965321}. Note=Has an amphipathic alpha-helical conformation in a lipid environment (Probable). May disrupt lipid membranes by forming pore-like structure (Probable). {ECO:0000305|PubMed:... | null | null | null | null | null | FUNCTION: Antimicrobial and chemotactic peptide for polymorphonucleated leukocytes (PMNL) (PubMed:16129513). Potent antimicrobial peptide against Gram-positive bacteria B.subtilis CCT 2576 (MIC=4 ug/ml), and S.aureus ATCC 6538 (MIC=15 ug/ml) and Gram-negative bacteria E.coli ATCC 25922 (MIC=8 ug/ml) and P.aeruginosa AT... | Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp) |
P0C1R0 | PROTO_POLPI | ILGTILGLLKSL | null | null | chemotaxis [GO:0006935]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; positive regulation of chemotaxis [GO:0050921] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | null | null | null | MCD family, Protonectin subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16129513}. Target cell membrane {ECO:0000269|PubMed:21745529, ECO:0000269|PubMed:22450985}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Is stable between 20 and 100 degrees Celsius. {ECO:0000269|PubMed:22450985}; | FUNCTION: Potent antimicrobial peptide that acts by disrupting bacterial membrane (PubMed:21745529, PubMed:22450985). Is active against both Gram-positive and Gram-negative bacteria (B.subtilis (MIC=15 ug/ml or 4-16 uM), S.epidermidis (MIC=8-16 uM), S.aureus (MIC=15 ug/ml or 4 uM), E.coli (MIC=8-64 uM) and P.aeruginosa... | Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp) |
P0C1R7 | CA1A_CONOM | GCCSHPACNVNNPHICG | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | PF07365; | null | Conotoxin A superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16803900}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=11 nM), alpha-7/CHRNA7 (IC(50)=27.1-59 nM (rat)/ 290 nM (human)), alpha-3-beta-4/CHRNA3-CHRNB4 (IC(50)=160 nM), and alpha-6/a... | Conus omaria (Omaria cone) |
P0C1S8 | WEE2_HUMAN | MDDKDIDKELRQKLNFSYCEETEIEGQKKVEESREASSQTPEKGEVQDSEAKGTPPWTPLSNVHELDTSSEKDKESPDQILRTPVSHPLKCPETPAQPDSRSKLLPSDSPSTPKTMLSRLVISPTGKLPSRGPKHLKLTPAPLKDEMTSLALVNINPFTPESYKKLFLQSGGKRKIRGDLEEAGPEEGKGGLPAKRCVLRETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSMKTFTELSNENSALHEVYAHAVLGHHPHVVRYYSSWAEDDHMIIQNEYCNGGSLQAAISENTKSGNHFEEPKLKDIL... | 2.7.10.2 | null | female meiotic nuclear division [GO:0007143]; female pronucleus assembly [GO:0035038]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of oocyte maturation [GO:1900194]; phosphorylation [GO:0016310]; positive regulation of phosphorylation ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylated on serine residues (PubMed:29606300). Phosphorylation leads to increase its activity (By similarity). {ECO:0000250|UniProtKB:Q66JT0, ECO:0000269|PubMed:29606300}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11029659, ECO:0000269|PubMed:29606300}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1/CDC2 and acts as a key regulator of meiosis during both prophase I and metaphase II (PubMed:29606300). Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate pr... | Homo sapiens (Human) |
P0C1S9 | DGLB_RAT | MPGMVLFGRRWSLASDDLVFPGSFELFLRVLWWIASLTLYLMHRRKLDCPGGVLLSTYLIVLLVLLAVIIGIVLAIVCVSMRGTICNPGPRKSMSKLLYIRLALFLPEMVWASLGAAWVAKGIQCDRTVVIGIIATVIVSWIVIAATMVTIVFVFDPLGGKMAPYPPCIPEHLDSNSSNHLLTGLRTAAKSVWETRVQCCCCCIGQDDNTRVAFSSTADLFSTYFSDTDLVPSDIAAGFTLLHQQQDKISHSREPSEVVTHTPGQPQETELDAEVENCHHYMPFSPVCSPWPVCVLNSSRVELCRTGNNFCRGRDIEYDA... | 3.1.1.116; 3.1.1.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q8NCG7}; | arachidonic acid metabolic process [GO:0019369]; cannabinoid biosynthetic process [GO:1901696]; diacylglycerol catabolic process [GO:0046340]; icosanoid metabolic process [GO:0006690]; monoacylglycerol biosynthetic process [GO:0006640]; neuroblast proliferation [GO:0007405]; neurogenesis [GO:0022008]; positive regulati... | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | acylglycerol lipase activity [GO:0047372]; lipase activity [GO:0016298]; metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806] | PF01764; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NCG7}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815, ChEBI:CHEBI:28868; EC=3.1.1.116; Evidence={ECO:0000250|UniProtKB:Q8NCG7}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | null | null | null | FUNCTION: Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production. P... | Rattus norvegicus (Rat) |
P0C1T0 | MMEL1_RAT | MGKSESSVGMMERADNCGRRRLGFVECGLLVLLTLLLMGAIVTLGVFYSIGKQLPLLNSLLHVSRHERTVVKRVLRDSSQKSDICTTPSCVIAAARILQNMDQSKKPCDNFYQYACGGWLRHHVIPETNSRYSVFDILRDELEVILKGVLEDSSVQHRPAVEKAKTLYRSCMNQSVIEKRDSEPLLNVLDMIGGWPVAMDKWNETMGPKWELERQLAVLNSQFNRRVLIDLFIWNDDQNSSRHVIYIDQPTLGMPSREYYFKEDSHRVREAYLQFMTSVATMLRRDLNLPGETDLVQEEMAQVLHLETHLANATVPQEKR... | 3.4.24.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | protein processing [GO:0016485]; proteolysis [GO:0006508] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886] | endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | PTM: N-glycosylated. {ECO:0000269|PubMed:11964170}. | SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Secreted. Note=A secreted form produced by proteolytic cleavage also exists. {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=62 uM for Tyrosyl-D-Ala(2)-Leu(5)-enkephalin {ECO:0000269|PubMed:11964170, ECO:0000269|PubMed:15294904}; KM=27 uM for Suc-AA-F-AMC (Membrane metallo-endopeptidase-like 1) {ECO:0000269|PubMed:11964170, ECO:0000269|PubMed:15294904}; KM=50 uM for Suc-AA-F-AMC (Membran... | null | null | null | FUNCTION: Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same su... | Rattus norvegicus (Rat) |
P0C1T1 | HXB2_MOUSE | MNFEFEREIGFINSQPSLAECLTSFPAVLETFQTSSIKESTLIPPPPPLEQTFPSLQLGASTLQRPGSQKQAGDGPALRSPPPLPVAPPAPEFPWMKEKKSTKKPSQSAASPSPAASSVRASEVGSPSDGPGLPECGGSGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPEGEPGGPSAQDDAGEPAEEPTVSPGDVATHRLREACFHPAEAAQGPRGAPPSALPATTLESVGASSPGCTMLRAGGRQSEPLPEDACPERQDSPFLPDLNFFAADSCLQMSGGL... | null | null | anterior/posterior pattern specification [GO:0009952]; dorsal/ventral pattern formation [GO:0009953]; embryonic skeletal system morphogenesis [GO:0048704]; facial nerve structural organization [GO:0021612]; morphogenesis of an epithelial sheet [GO:0002011]; neural nucleus development [GO:0048857]; rhombomere 3 developm... | nucleoplasm [GO:0005654] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Antp homeobox family, Proboscipedia subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. {ECO:0000250|UniProtKB:P14652}. | Mus musculus (Mouse) |
P0C1U8 | SSPA_STAAU | MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPD... | 3.4.21.19 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type endopeptidase activity [GO:0004252] | PF13365; | 2.40.10.10; | Peptidase S1B family | PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4627743}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10083}; | null | null | null | null | FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It i... | Staphylococcus aureus |
P0C1V7 | CA1AB_CONAN | GGCCSHPACAANNQDYC | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Conotoxin A superfamily | PTM: C-terminal amidation, in synergy with sulfation, is important for activity and structure stability (PubMed:14971903, PubMed:34671739). Non-amidated conotoxins has a 1.9-fold lower inhibitory potency on alpha-3-beta-2/CHRNA3-CHRNB2 nAChRs (IC(50)=0.54 nM), and a 4.8-fold lower inhibitory potency on alpha-7/CHRNA7 n... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14971903}. | null | null | null | null | null | FUNCTION: [Alpha-conotoxin AnIB]: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This synthetic toxin blocks rat alpha-3beta-2/CHRNA3-CHRNB2 nAChRs (IC(50)=0.3 nM) and alpha-7/CHRNA7 nAChRs (IC(50)=76 nM). {ECO:0000269|PubMed:14971903}.;... | Conus anemone (Anemone cone) |
P0C1W5 | CDKA_CONVX | MPKLEMMLLVLLIFPLSYFIAAGGQVVQVDRRGDGLAGYLQRGDRDVQDCQVSTPGSKWGRCCLNRVCGPMCCPASHCYCVYHRGRGHGCSC | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Conotoxin D superfamily | PTM: VxXXA stands for the form with the Pro-55 hydroxylated. A second major form has both Pro-55 and Pro-74 hydroxylated. The two major forms VxXXA and [hydroxyPro-74]VxXXA exist in a 1:1 ratio. {ECO:0000269|PubMed:16790424}.; PTM: Minor forms are [hydroxyPro-70,hydroxyPro-74]VxXXA and [Pro-55]VxXXA. {ECO:0000269|PubMe... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16790424}. | null | null | null | null | null | FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Through its two C-terminal domains, this homodimeric protein would bind to two nAChR allosteric sites, located outside the nAChR C-loop of the principal binding face and at the adj... | Conus vexillum (Flag cone) |
P0C1W6 | CDKB_CONVX | MPKLAVVLLVLLILPLSYFDAAGGQAVQGDWRGNRLARDLQRGGRDDESECIINTRDSPWGRCCRTRMCGSMCCPRNGCTCVYHWRRGHGCSCPG | null | null | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | acetylcholine receptor inhibitor activity [GO:0030550]; ion channel regulator activity [GO:0099106]; toxin activity [GO:0090729] | null | null | Conotoxin D superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16790424}. | null | null | null | null | null | FUNCTION: [Alpha-conotoxin VxXXB]: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Through its two C-terminal domains, this homodimeric protein would bind to two nAChR allosteric sites, located outside the nAChR C-loop of the principal bi... | Conus vexillum (Flag cone) |
P0C1X8 | AAK1_RAT | MKKFFDSRREQGSSGLGSGSSGGGGSSSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFALVFLVRTSNGVKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQAEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGSFTIPDNSRYSQDMHCLIYMLEPDPDKRPDIYQVSYFSFKLLKKECPV... | 2.7.11.1 | null | phosphorylation [GO:0016310]; positive regulation of Notch signaling pathway [GO:0045747]; presynaptic endocytosis [GO:0140238]; protein stabilization [GO:0050821]; regulation of clathrin-dependent endocytosis [GO:2000369]; regulation of protein localization [GO:0032880] | calyx of Held [GO:0044305]; cell leading edge [GO:0031252]; clathrin complex [GO:0071439]; clathrin-coated pit [GO:0005905]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; synapse [GO:0045202]; terminal bouton [GO:0043195] | AP-2 adaptor complex binding [GO:0035612]; ATP binding [GO:0005524]; Notch binding [GO:0005112]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q2M2I8}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:F1MH24}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11877461}. Presynapse {ECO:0000269|PubMed:11877461}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells,... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis (PubMed:11877461). Preferentially, may phosphorylate substrates on threonine ... | Rattus norvegicus (Rat) |
P0C1Z0 | 3SE2_DENAN | TMCYSHTTTSRAILTNCGENSCYRKSRRHPPKMVLGRGCGCPPGDDNLEVKCCTSPDKCNY | null | null | null | extracellular region [GO:0005576] | toxin activity [GO:0090729] | null | 2.10.60.10; | Snake three-finger toxin family, Short-chain subfamily, Acn-esterase inhibitor sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4123919}. | null | null | null | null | null | FUNCTION: Interferes with neuromuscular transmission by inhibiting the enzyme acetylcholinesterase (AChE) present at the neuromuscular junction. It selectively binds and inhibits with a 1:1 stoichiometry the mammalian and electric fish AChE at picomolar concentrations. It is highly specific for the peripheral site of A... | Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps) |
P0C1Z6 | TFPT_HUMAN | MELEQREGTMAAVGFEEFSAPPGSELALPPLFGGHILESELETEVEFVSGGLGGSGLRERDEEEEAARGRRRRQRELNRRKYQALGRRCREIEQVNERVLNRLHQVQRITRRLQQERRFLMRVLDSYGDDYRASQFTIVLEDEGSQGTDAPTPGNAENEPPEKETLSPPRRTPAPPEPGSPAPGEGPSGRKRRRVPRDGRRAGNALTPELAPVQIKVEEDFGFEADEALDSSWVSRGPDKLLPYPTLASPASD | null | null | apoptotic signaling pathway [GO:0097190]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; male gonad development [GO:0008584]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcrip... | actin filament [GO:0005884]; cytoplasm [GO:0005737]; Ino80 complex [GO:0031011]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922472}. | null | null | null | null | null | FUNCTION: Appears to promote apoptosis in a p53/TP53-independent manner.; FUNCTION: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. | Homo sapiens (Human) |
P0C205 | REX_HTL1A | MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPSRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPT | null | null | mRNA transport [GO:0051028] | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | RNA binding [GO:0003723] | null | null | Deltaretrovirus Rex protein family | null | SUBCELLULAR LOCATION: [Isoform Rex]: Host nucleus, host nucleolus. Host cytoplasm. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm.; SUBCELLULAR LOCATION: [Isoform p21Rex]: Host cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Rex escorts unspliced gag-pro-pol and singly spliced env mRNAs out of the nucleus of infected cells. These mRNAs carry a recognition sequence called Rex responsive element (RxRE or XRE) located at the 3' region of the long terminal repeat (LTR). This function is essential since most HTLV proteins are translat... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P0C206 | REX_HTL1C | MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPLRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPM | null | null | mRNA transport [GO:0051028] | host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | RNA binding [GO:0003723] | null | null | Deltaretrovirus Rex protein family | PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform Rex]: Host nucleus, host nucleolus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform p21Rex]: Host cytoplasm {ECO:... | null | null | null | null | null | FUNCTION: Rex escorts unspliced gag-pro-pol and singly spliced env mRNAs out of the nucleus of infected cells. These mRNAs carry a recognition sequence called Rex responsive element (RxRE or XRE) located at the 3' region of the long terminal repeat (LTR). This function is essential since most HTLV proteins are translat... | Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1) |
P0C209 | GAG_HTL1L | MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | null | null | viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03345}.; PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P03345}.... | Human T-cell leukemia virus 1 (isolate Melanesia mel5 subtype C) (HTLV-1) |
P0C210 | PRO_HTL1L | MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | 3.4.23.- | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P10274}.; PTM: [Matrix protein p19]:... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P033... | Human T-cell leukemia virus 1 (isolate Melanesia mel5 subtype C) (HTLV-1) |
P0C211 | POL_HTL1L | MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion bi... | PF02228;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF00098; | 1.10.1200.30;3.30.70.270;2.40.70.10;1.10.185.10;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and i... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CH... | null | null | null | null | FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:... | Human T-cell leukemia virus 1 (isolate Melanesia mel5 subtype C) (HTLV-1) |
P0C215 | P12I_HTL1A | MLFRLLSPLSPLALTALLLFLLPPSDVSGLLLRPPPAPCLLLFLPFQILSGLLFLLFLPLFFSLPLLLSPSLPITMRFPARWRFLPWKAPSQPAAAFLF | null | null | symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi apparatus [GO:0044177]; membrane [GO:0016020] | SH3 domain binding [GO:0017124] | PF12233; | null | HTLV-1 accessory protein p12I family | PTM: Ubiquitinated; a fraction of P12I is degraded via the ubiquitin system. {ECO:0000269|PubMed:10400740}. | SUBCELLULAR LOCATION: [Isoform p12I]: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Host Golgi apparatus, host cis-Golgi network membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: p12I is a modulator of T-lymphocyte proliferation and immune function and may contribute to establish a persistent infection. Binds and down-modulates cell surface expression of interleukin-2 receptors IL2RB and IL2RG. Also down-modulates cell surface MHC-I molecules by binding to free immature MHC-I heavy ch... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P0C216 | PHLC1_CLOPE | MKRKICKALICATLATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEM... | 3.1.4.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000305}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 3 Zn(2+) ions per subunit.; | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | calcium-dependent phospholipase C activity [GO:0050429]; phosphatidylcholine phospholipase C activity [GO:0034480]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF01477;PF00882; | 1.10.575.10;2.60.60.20; | Bacterial zinc-metallophospholipase C family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3; | null | null | null | null | FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic aci... | Clostridium perfringens (strain 13 / Type A) |
P0C225 | OSTCN_CAPHI | YLDPGLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGIA | null | null | biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast diffe... | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity) (PubMed:6332627). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463, ECO:... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6332627}. | null | null | null | null | null | FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (PubMed:6332627). It acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated for... | Capra hircus (Goat) |
P0C226 | OSTCN_NOTEU | YLYQTLGFPAPYPDPQENKREVCELNPDCDELADHIGFQEAYRRFYGTA | null | null | biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast diffe... | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147] | null | null | Osteocalcin/matrix Gla protein family | PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity) (PubMed:6332627). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463, ECO:... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6332627}. | null | null | null | null | null | FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly ... | Notamacropus eugenii (Tammar wallaby) (Macropus eugenii) |
P0C247 | JZ11A_CHIGU | MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSGERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}. | null | null | null | null | null | FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases th... | Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao) |
P0C248 | COW_CONAA | MGKLTILVLVAAALLSTQVMVQGDGDQPADRDAVPRDDNPSGMSGKFMNVLRRAGCPWDPWCG | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729] | PF02950; | null | O2 superfamily, Contryphan family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16387709, ECO:0000269|PubMed:16945451, ECO:0000269|PubMed:17902199}. | null | null | null | null | null | FUNCTION: Inhibits high voltage-activated calcium channels (Cav). {ECO:0000269|PubMed:16945451}. | Conus amadis (Amadis cone) |
P0C250 | COW1_CONBL | MGKLTILVLVAAVLLSTQVMVQGDGDQPADRNAVRRDDNPGGTRGRFMNILRRTGCPWDPWCG | null | null | null | extracellular region [GO:0005576] | calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729] | PF02950; | null | O2 superfamily, Contryphan family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16387709, ECO:0000269|PubMed:16945451}. | null | null | null | null | null | FUNCTION: Activates high voltage-activated calcium channels (Cav). This activity is in contrast to other contryphans that inhibit high voltage-gated calcium channels. {ECO:0000269|PubMed:16945451}. | Conus buxeus loroisii (Cone snail) (Conus loroisii) |
P0C264 | SBK3_HUMAN | MERRASETPEDGDPEEDTATALQRLVELTTSRVTPVRSLRDQYHLIRKLGSGSYGRVLLAQPHQGGPAVALKLLRRDLVLRSTFLREFCVGRCVSAHPGLLQTLAGPLQTPRYFAFAQEYAPCGDLSGMLQERGLPELLVKRVVAQLAGALDFLHSRGLVHADVKPDNVLVFDPVCSRVALGDLGLTRPEGSPTPAPPVPLPTAPPELCLLLPPDTLPLRPAVDSWGLGVLLFCAATACFPWDVALAPNPEFEAFAGWVTTKPQPPQPPPPWDQFAPPALALLQGLLDLDPETRSPPLAVLDFLGDDWGLQGNREGPGVL... | 2.7.11.1 | null | phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, STKL subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | null | Homo sapiens (Human) |
P0C276 | RL40_SHEEP | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRQLAQKYNCDKMICRKCYARLHPRAVNCRKKKCGHTNNLRPKKKVK | null | null | modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]; translation [GO:0006412] | cytosolic large ribosomal subunit [GO:0022625]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202] | protein tag activity [GO:0031386]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF01020;PF00240; | 4.10.1060.50; | Ubiquitin family; Eukaryotic ribosomal protein eL40 family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects de... | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Ovis aries (Sheep) |
P0C278 | FCCA_SHEFR | ADNLAEFHVQNQECDSCHTPDGELSNDSLTYENTQCVSCHGTLEEVAETTKHEHYNAHASHFPGEVACTSCHSAHEKSMVYCDSCHSFDFNMPYAKKWQRDEPTIAELAKDKSERQAALASAPHDTVDVVVVGSGGAGFSAAISATDSGAKVILIEKEPVIGGNAKLAAGGMNAAWTDQQKAKKITDSPELMFEDTMKGGQNINDPALVKVLSSHSKDSVDWMTAMGADLTDVGMMGGASVNRAHRPTGGAGVGAHVVQVLYDNAVKRNIDLRMNTRGIEVLKDDKGTVKGILVKGMYKGYYWVKADAVILATGGFAKNN... | 1.3.2.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10978153}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10978153}; COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:10978153}; Note=Binds 4 heme c groups covalently per monomer. {ECO:0000269|PubMed:10978153}; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; steroid metabolic process [GO:0008202] | outer membrane-bounded periplasmic space [GO:0030288] | electron transfer activity [GO:0009055]; FMN binding [GO:0010181]; metal ion binding [GO:0046872]; succinate dehydrogenase (quinone) activity [GO:0008177] | PF14537;PF00890; | 3.50.50.60;3.90.700.10; | FAD-dependent oxidoreductase 2 family, FRD/SDH subfamily | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + succinate = 2 Fe(II)-[cytochrome c] + fumarate + 2 H(+); Xref=Rhea:RHEA:77903, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031; EC=1.3.2.4; Evidence={ECO:0000305|PubMed:10978... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43 uM for fumarate (at pH 6.0 with methyl viologen as electron donor) {ECO:0000269|PubMed:10978153}; KM=25 uM for fumarate (at pH 7.2 with methyl viologen as electron donor) {ECO:0000269|PubMed:10978153}; KM=28 uM for fumarate (at pH 7.5 with methyl viologen as ele... | null | null | null | FUNCTION: Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:10978153). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (By similarity). In vitro, can u... | Shewanella frigidimarina |
P0C279 | CPEB1_RAT | MAFSLEEESGRIKDCWDNQEVPALSTCSNANIFRRINAILDDSLDFSKVCTTPINRGIHDQLPDFQDSEEAITSRMLFPTSAQESPRGLPDANGLCLGLQSLSLTGWDRPWSTQDSDSSAQSNTQSVLSMLQNPLGNVLGKTPLSFLSLDPLGSDLDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSMTGNGPRDPLKMGVGSRMDQEQAALAAVAPSPTSAPKRWPGTSVWPSWDLLGAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWD... | null | null | cellular response to amino acid stimulus [GO:0071230]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to lipopolysaccharide [GO:0071222]; mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; negative regulation of cell population proliferation [GO:... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; meiotic spindle [GO:0072687]; membrane [GO:0016020]; messenger ribonucleoprotein complex [GO:1990124]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; P-body [GO:0000932]... | metal ion binding [GO:0046872]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; mRNA regulatory element binding translation repressor activity [GO:0000900]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation factor activity, RNA binding [GO... | PF16368;PF16366;PF16367; | 3.30.70.330;4.10.640.40; | RRM CPEB family | PTM: Phosphorylated on serine/threonine residues by AURKA within positions 165 and 196. Phosphorylation and dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-171 by AURKA and CAMK2A activates CPEB1. Phosphorylation on Thr-171 may be promot... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Membrane {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Localizes in synaptosomes at dendritic synapses of neurons. Strongly enriched in postsynaptic density fractions. Tran... | null | null | null | null | null | FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUU... | Rattus norvegicus (Rat) |
P0C2C2 | RBL1C_CUPNE | MNAPETIQAKPRKRYDAGVMKYKEMGYWDGDYVPKDTDVLALFRITPQDGVDPVEAAAAVAGESSTATWTVVWTDRLTACDMYRAKAYRVDPVPNNPEQFFCYVAYDLSLFEEGSIANLTASIIGNVFSFKPIKAARLEDMRFPVAYVKTFAGPSTGIIVERERLDKFGRPLLGATTKPKLGLSGRNYGRVVYEGLKGGLDFMKDDENINSQPFMHWRDRFLFVMDAVNKASAATGEVKGSYLNVTAGTMEEMYRRAEFAKSLGSVIIMVDLIVGWTCIQSMSNWCRQNDMILHLHRAGHGTYTRQKNHGVSFRVIAKWL... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; | reductive pentose-phosphate cycle [GO:0019253] | null | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: A disulfide bond might be able to form between Cys-278 in the large chain dimeric partners within the hexadecamer. {ECO:0000305|PubMed:10329167}. | null | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglyce... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. | Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) |
P0C2D1 | OXLA_BOTPI | ADDKNPLEEFRETNYEVFLEIAKNGLKATSNPKRVVIVGAGMAGLSAAY | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | 3.50.50.60; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.; PTM: N-glycosylated. {ECO:0000305|PubMed:16809041}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16809041}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:16809041}; CATALYTIC ACTIVITY: Reaction=H2O... | null | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:16809041). Is highly active on L-Phe, L-Tyr, L-Trp, L-Leu, L-Met, and L-Ile, is moderately active on L-Val, and L... | Bothrops pirajai (Piraja's lancehead) |
P0C2D4 | OXLA_NAJKA | DDRRSPLEECFQQNDYEEFLEIAKNGLKKTXNPKHVXV | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | 3.90.660.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11600144, ECO:0000269|PubMed:1612186}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:1612186}; CATALYTIC ACTIVITY: Reaction=H2O ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.023 mM for L-Tyr {ECO:0000269|PubMed:1612186}; KM=0.06 mM for L-Phe {ECO:0000269|PubMed:1612186}; KM=0.29 mM for L-Trp {ECO:0000269|PubMed:1612186}; KM=0.63 mM for L-Met {ECO:0000269|PubMed:1612186}; KM=0.66 mM for L-Leu {ECO:0000269|PubMed:1612186}; KM=1.69 mM f... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5, unlike many other venom L-amino acid oxidase, is also stable in alkaline medium. {ECO:0000269|PubMed:1612186}; | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:1612186). Is very active against L-Phe and L-Tyr, moderately active against L-Trp, L-Met, L-Leu, L-norleucine (L-... | Naja kaouthia (Monocled cobra) (Naja siamensis) |
P0C2D7 | OXLA_VIPBB | ADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVYPVKPSEQLYEESLRDQLPTSMHRYPSMIQKIFFAGEYTANAHGWIDSTIK | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-glutamate oxidase activity [GO:0050025]; L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | null | 3.90.660.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16574513}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:16574513}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.361 mM for L-Leu {ECO:0000269|PubMed:16574513}; KM=0.286 mM for L-Met {ECO:0000269|PubMed:16574513}; KM=0.058 mM for L-Phe {ECO:0000269|PubMed:16574513}; | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:16574513). Is highly active on L-Met, L-Leu, L-Phe, L-Ile, and L-Arg, moderately active on L-His, L-Trp, L-Asn, L... | Vipera berus berus (Common viper) |
P0C2E9 | TACY_CLOPE | MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTA... | null | null | hemolysis in another organism [GO:0044179] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | cholesterol binding [GO:0015485]; toxin activity [GO:0090729] | PF17440;PF01289; | 3.30.1040.20;3.40.30.40;2.60.40.1430;3.90.840.10; | Cholesterol-dependent cytolysin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2878682}. Host cell membrane; Multi-pass membrane protein {ECO:0000305|PubMed:15851031}. Note=Secreted as soluble protein that then inserts into the host cell membrane and forms huge pores formed by transmembrane beta-strands. {ECO:0000305|PubMed:15851031}. | null | null | null | null | null | FUNCTION: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol-containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A major conformational change leads to insertion in the host membrane and formation of an oligomeric pore complex. Ch... | Clostridium perfringens (strain 13 / Type A) |
P0C2H4 | DSE_BOVIN | MRTHTRGAPSVFFICLFCFVSACVTDENPEVMIPFTNANYDSHPMLYFSRAEVAELQLRAASSHEHIAARLTEAVNTMLSSPLEYLPPWDPKEYSARWNEIYGNNLGALAMFCVLYPENMEARDMAKDYMERMAAQPSWLVKDAPWDEVPLAHSLVGFATAYDFLYNYLSKTQQEKFLEVIANASGYMYETSYRRGWGFQYLHNHQPTNCMALLTGSLVLMNQGYLQEAYLWTKQVLTIMEKSLVLLREVTDGSLYEGVAYGSYTTRSLFQYMFLVQRHFDINHFGHPWLKQHFAFMYRTILPGFQRTVAIADSNYNWFY... | 5.1.3.19 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UL01}; Note=Also has weak activity in the presence of Mg(2+) or Ca(2+) ions. {ECO:0000250|UniProtKB:Q9UL01}; | chondroitin sulfate biosynthetic process [GO:0030206]; chondroitin sulfate metabolic process [GO:0030204]; dermatan sulfate metabolic process [GO:0030205]; heparan sulfate proteoglycan biosynthetic process [GO:0015012] | cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | chondroitin-glucuronate 5-epimerase activity [GO:0047757]; metal ion binding [GO:0046872] | PF16332; | 2.70.98.70;1.50.10.100; | Dermatan-sulfate isomerase family | PTM: N-glycosylated. Glycosylation is important for enzymatic activity. {ECO:0000250|UniProtKB:Q9UL01}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:16505484}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UL01}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UL01}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UL01}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9UL01}... | CATALYTIC ACTIVITY: Reaction=chondroitin 4'-sulfate = dermatan 4'-sulfate; Xref=Rhea:RHEA:21084, Rhea:RHEA-COMP:9829, Rhea:RHEA-COMP:9965, ChEBI:CHEBI:58422, ChEBI:CHEBI:58465; EC=5.1.3.19; Evidence={ECO:0000305|PubMed:16505484}; | null | PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis. {ECO:0000305|PubMed:16505484}.; PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000305|PubMed:16505484}. | null | null | FUNCTION: Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. Plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide dermatan sulfate. {ECO:0000269|PubMed:16505484}. | Bos taurus (Bovine) |
P0C2I2 | YD14B_YEAST | MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2I3 | YD15B_YEAST | MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2I5 | YL12B_YEAST | MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2I6 | YL13B_YEAST | MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2I7 | YL14B_YEAST | MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; transposition [GO:0032196] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2I9 | YP12B_YEAST | MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2J0 | YP13B_YEAST | MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2J1 | YP14B_YEAST | MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGE... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2J3 | YL21B_YEAST | MESQQLHQNPHSLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDLKNQHSEIPQAKTKVGNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKRQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYL... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2J5 | YL22B_YEAST | MESQQLHQNPHSLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQEETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDSQDQHSEVPQAKTKVRNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKRQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYSDILTVLCKSVSKMQTNNQELKDWIALANLEYNGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYL... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; transposition [GO:0032196] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00665;PF07727;PF01021; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the part... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2J7 | YH41B_YEAST | MATPVRDETRNVIDDNISARIQSKVKTNDTVRQTPSSLRKVSIKDEQVKQYQRNLNRFKTILNGLKAEEEKLSETDDIQMLAEKLLKLGETIDKVENRIVDLVEKIQLLETNENNNILHEHIDATGTYYLFDTLTSTNKRFYPKDCVFDYRTNNVENIPILLNNFKKFIKKYQFDDVFENDIIEIDPRENEILCKIIKEGLGESLDIMNTNTTDIFRIIDGLKNKYRSLHGRDVRIRAWEKVLVDTTCRNSALLMNKLQKLVLMEKWIFSKCCQDCPNLKDYLQEAIMGTLHESLRNSVKQRLYNIPHNVGINHEEFLIN... | 2.7.7.49; 2.7.7.7; 3.1.26.4; 3.4.23.- | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; proteolysis [GO:0006508]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | aspartic-type endopeptidase activity [GO:0004190]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [G... | PF00665;PF07727; | 3.30.420.10; | null | PTM: Proteolytically processed into capsid protein (CA), Ty4 protease (PR), integrase (IN) and reverse transcriptase/ribonuclease H (RT) proteins (Probable). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (t... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n)... | null | null | null | null | FUNCTION: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. {ECO:0000250}.; FUNCTION: The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C2N5 | KMT5B_RAT | MKWLGDSKNMVVNGRRNGSKLSNDHQQNQSKLQHAGKDALKTGRNAVERRPNRCHGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHISKADSFSHNNPMRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCE... | 2.1.1.361; 2.1.1.362 | null | DNA repair [GO:0006281]; methylation [GO:0032259]; muscle organ development [GO:0007517]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034]; positive regulation of isotype switching [GO:0045830] | condensed chromosome, centromeric region [GO:0000779]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone H4K20 methyltransferase activity [GO:0042799]; histone H4K20 monomethyltransferase activity [GO:0140944]; histone H4K20me methyltransferase activity [GO:0140941]; histone methyltransferase activity [GO:0042054]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:... | PF00856; | 1.10.10.1700;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar4-20 subfamily | null | SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}. Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEB... | null | null | null | null | FUNCTION: Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In v... | Rattus norvegicus (Rat) |
P0C2N6 | KMT5C_RAT | MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPTLRRQHHLRSALEAFLRQRDLEAAFRALTLGGWMAHYFQNRAPRQEAALKNHIFCYLRAFLPESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEYLLRAGENDFSVMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGEGAFRLQPREPELRPRPLDKYELRETKRRLQQCLDSSQQNLLSLRACSHLSPLRPDPFCAACQPSCLLPVSPHMDYLPLWLQ... | 2.1.1.361; 2.1.1.362 | null | DNA repair [GO:0006281]; methylation [GO:0032259]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034]; positive regulation of isotype switching [GO:0045830] | condensed chromosome, centromeric region [GO:0000779]; heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; histone H4K20 methyltransferase activity [GO:0042799]; histone H4K20 monomethyltransferase activity [GO:0140944]; histone H4K20me methyltransferase activity [GO:0140941]; metal ion binding [GO:0046872]; S-adenosyl-L-methionine binding [GO:1904047] | PF00856; | 1.10.10.1700;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar4-20 subfamily | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin. | CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEB... | null | null | null | null | FUNCTION: Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In v... | Rattus norvegicus (Rat) |
P0C2P0 | BSD_ASPTE | MPLSQEESTLIERATATINSIPISEDYSVASAALSSDGRIFTGVNVYHFTGGPCAELVVLGTAAAAAAGNLTCIVAIGNENRGILSPCGRCRQVLLDLHPGIKAIVKDSDGQPTAVGIRELLPSGYVWEG | 3.5.4.23 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; | response to antibiotic [GO:0046677] | cytosol [GO:0005829] | blasticidin-S deaminase activity [GO:0047711]; cytidine deaminase activity [GO:0004126]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF00383; | 3.40.140.10; | Cytidine and deoxycytidylate deaminase family | null | null | CATALYTIC ACTIVITY: Reaction=blasticidin S + H(+) + H2O = deaminohydroxyblasticidin S + NH4(+); Xref=Rhea:RHEA:10148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57289, ChEBI:CHEBI:57697; EC=3.5.4.23; | null | null | null | null | FUNCTION: Catalyzes the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S. | Aspergillus terreus |
P0C2S4 | GUND_ACETH | SLTGVFPSGLIETKVSAAKITENYQFDSRIRLNSIGFIPNHSKKATIAANCSTFYVVKEDGTIVYTGTATSMFDNDTKETVYIADFSSVNEEGTYYLAVPGVGKSVNFKIAMNVYEDAFKTAMLGMYLLRCGTSVSATYNGIHYSHGPCHTNDAYLDYINGQHTKKDSTKGWHDAGDYNKYVVNAGITVGSMFLAWEHFKDQLEPVALEIPEKNNSIPDFLDELKYEIDWILTMQYPDGSGRVAHKVSTRNFGGFIMPENEHDERFFVPWSSAATADFVAMTAMAARIFRPYDPQYAEKCINAAKVSYEFLKNNPANVFA... | 3.2.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; | cellulose catabolic process [GO:0030245] | null | cellulase activity [GO:0008810] | PF02927;PF00404;PF00759; | 1.50.10.10;1.10.1330.10;2.60.40.10; | Glycosyl hydrolase 9 (cellulase E) family | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; | null | null | null | null | FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. | Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
P0C2S5 | GUNS_ACETH | MVKSRKISILLAVAMLVSIMIPTTAFAGPTKAPTKDGTSYKDLFLELYGKIKDPKNGYFSPDEGIPYHSIETLIVEAPDYGHVTTSEAFSYYVWLEAMYGNLTGNWSGVETAWKVMEDWIIPDSTEQPGMSSYNPNSPATYADEYEDPSYYPSELKFDTVRVGSDPVHNDLVSAYGPNMYLMHWLMDVDNWYGFGTGTRATFINTFQRGEQESTWETIPHPSIEEFKYGGPNGFLDLFTKDRSYAKQWRYTNAPDAEGRAIQAVYWANKWAKEQGKGSAVASVVSKAAKMGDFLRNDMFDKYFMKIGAQDKTPATGYDSA... | 3.2.1.176 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose 1,4-beta-cellobiosidase activity (reducing end) [GO:0102252]; metal ion binding [GO:0046872] | PF00404;PF02011; | 1.50.10.10;1.10.1330.10;2.170.160.10;4.10.870.10; | Glycosyl hydrolase 48 (cellulase L) family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.; EC=3.2.1.176; Evidence={ECO:0000269|PubMed:20967294}; | null | null | null | null | FUNCTION: This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose. {ECO:0000269|PubMed:20967294}. | Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum) |
P0C2T2 | A85B_MYCBO | MTDVSRKIRAWGRRLMIGTAAAVVLPGLVGLAGGAATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETFLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQS... | 2.3.1.122; 2.3.1.20 | null | null | extracellular region [GO:0005576] | diacylglycerol O-acyltransferase activity [GO:0004144]; trehalose O-mycolyltransferase activity [GO:0050348] | PF00756; | 3.40.50.1820; | Mycobacterial A85 antigen family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose 6,6'-bismycolate + alpha,alpha-trehalose; Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195, ChEBI:CHEBI:18234; EC=2.3.1.122; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + C... | null | null | null | null | FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of Mycobacteria to murine alveolar macrophages (AMs) (PubMed:8406884). They also help to maintain the integrity of the cell wall by ... | Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) |
P0C2T7 | PEPT_LACLC | MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIQLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNMMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPLIK... | 3.4.11.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:16348224}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305|PubMed:16348224}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytosol [GO:0005829] | metallopeptidase activity [GO:0008237]; tripeptide aminopeptidase activity [GO:0045148]; zinc ion binding [GO:0008270] | PF07687;PF01546; | 3.30.70.360;3.40.630.10; | Peptidase M20B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Release of the N-terminal residue from a tripeptide.; EC=3.4.11.4; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for tripeptide Leu-Leu-Leu {ECO:0000269|PubMed:16348224}; Vmax=151 umol/min/mg enzyme with Leu-Leu-Leu as substrate {ECO:0000269|PubMed:16348224}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16348224}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:16348224}; | FUNCTION: Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides. {ECO:0000269|... | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
P0C2W1 | FBSP1_HUMAN | MAAPAPGAGAASGGAGCSGGGAGAGAGSGSGAAGAGGRLPSRVLELVFSYLELSELRSCALVCKHWYRCLHGDENSEVWRSLCARSLAEEALRTDILCNLPSYKAKIRAFQHAFSTNDCSRNVYIKKNGFTLHRNPIAQSTDGARTKIGFSEGRHAWEVWWEGPLGTVAVIGIATKRAPMQCQGYVALLGSDDQSWGWNLVDNNLLHNGEVNGSFPQCNNAPKYQIGERIRVILDMEDKTLAFERGYEFLGVAFRGLPKVCLYPAVSAVYGNTEVTLVYLGKPLDG | null | null | anterior commissure morphogenesis [GO:0021960]; cerebral cortex radially oriented cell migration [GO:0021799]; cerebral cortex tangential migration [GO:0021800]; corticospinal tract morphogenesis [GO:0021957]; DNA damage response [GO:0006974]; neuron migration [GO:0001764]; proteasome-mediated ubiquitin-dependent prote... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; postsynaptic cytosol [GO:0099524]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; presynaptic cytosol [GO:0099523]; presynaptic membrane [GO:0042734]... | ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF12937;PF00622; | 1.20.1280.50;2.60.120.920; | FBXO45/Fsn family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32341084}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P0CH38}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P0CH38}. Nucleus {ECO:0000269|PubMed:26068074}. Note=Secreted by a non-classical mechanism. {ECO:0000269|PubMed:32341084}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of E3 ubiquitin ligase complex consisting of FBXO45, MYCBP2 and SKP1 (PubMed:29997255). Functions in substrate recognition but plays also an important role in assembly of the complex (PubMed:29997255). Required for normal neuromuscular synaptogenesis, axon pathfinding and neuronal migration (By simi... | Homo sapiens (Human) |
P0C2W5 | GBRB2_BOVIN | RVRKKDYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTTACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLE... | null | null | cellular response to histamine [GO:0071420]; chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; inhibitory synapse assembly [GO:1904862]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRB2 sub-subfamily | PTM: Glycosylated. {ECO:0000250|UniProtKB:P63137}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P63137}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cell membrane {ECO:0000269|PubMed:17093081, ECO:0000269|PubMed:2548852}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cytoplasmic vesicle membrane {ECO:0000250|UniP... | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P08219}; | null | null | null | null | FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:2548852). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contai... | Bos taurus (Bovine) |
P0C349 | CM3C_CONST | RHGCCKGPKGCSSRECRPQHCC | null | null | null | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF05374; | null | Conotoxin M superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17142296}. | null | null | null | null | null | FUNCTION: Mu-conotoxins block voltage-gated sodium channels. This synthetic peptide reversibly inhibits the brain sodium channel rNav1.2/SCN2A (IC(50) is 40 nM) and the skeletal muscle sodium channel rNav1.4/SCN4A (IC(50) is 9 nM). {ECO:0000269|PubMed:17142296}. | Conus striatus (Striated cone) |
P0C350 | CM3A_CONTU | RHGCCKGPKGCSSRECRPQHCC | null | null | null | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF05374; | null | Conotoxin M superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). This synthetic toxin reversibly and potently blocks rNav1.4/SCN4A (IC(50) is 9 nM) and rNav1.2/SCN2A (IC(50) is 40 nM). It also moderately blocks rNav1.1/SCN1A, rNav1.3/SCN3A, and rNav1.6/SCN8A. The block of SCN1A and SCN2A is modified when beta-subunit... | Conus tulipa (Fish-hunting cone snail) (Tulip cone) |
P0C511 | RBL_ORYSI | MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRM... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507]; plastid [GO:0009536] | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000250}. | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglyce... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By s... | Oryza sativa subsp. indica (Rice) |
P0C512 | RBL_ORYSJ | MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRM... | 4.1.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22609438}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:22609438}; | photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253] | chloroplast [GO:0009507]; plastid [GO:0009536] | magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; nucleotide binding [GO:0000166]; ribulose-bisphosphate carboxylase activity [GO:0016984] | PF00016;PF02788; | 3.20.20.110;3.30.70.150; | RuBisCO large chain family, Type I subfamily | PTM: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bond reported in 1WDD may be the result of oxidation during crystallization. {ECO:0000250|UniProtKB:P11383}... | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglyce... | null | null | null | null | FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Oryza sativa subsp. japonica (Rice) |
P0C548 | PLPL2_RAT | MFPRETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFNLVKTIRGCLLKTLPADCHTRASGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRITNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRFLRRNGLLNQPNPLLALPPVVPQEEDAEEAAVTEERTGGEDRILEHLPARLNEALLEACVEPKDLMTTLSNML... | 3.1.1.3; 3.1.1.4 | null | cellular lipid catabolic process [GO:0044242]; diacylglycerol biosynthetic process [GO:0006651]; lipid droplet disassembly [GO:1905691]; lipid droplet organization [GO:0034389]; lipid homeostasis [GO:0055088]; lipid storage [GO:0019915]; negative regulation of sequestering of triglyceride [GO:0010891]; positive regulat... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | acylglycerol O-acyltransferase activity [GO:0016411]; diolein transacylation activity [GO:0051265]; mono-olein transacylation activity [GO:0051264]; phospholipase A2 activity [GO:0004623]; retinyl-palmitate esterase activity [GO:0050253]; triglyceride lipase activity [GO:0004806] | PF01734; | 3.40.1090.10; | null | PTM: Phosphorylation at Ser-398 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity. {ECO:0000250|UniProtKB:Q8BJ56}.; PTM: Ubiquitinated by PEX2 in response to reactive oxygen species (ROS), leading to its degradation. {ECO:0000250|UniProtKB:Q96AD5}. | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q96AD5}. Cell membrane {ECO:0000250|UniProtKB:Q96AD5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BJ56}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:Q96AD5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12... | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. | null | null | FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (By similarity). Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic ... | Rattus norvegicus (Rat) |
P0C559 | GYRB_MYCSM | MAAQKNNAPKEYGADSITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGFATRVDVKIHADGSVEVRDDGRGIPVEMHATGMPTIDVVMTQLHAGGKFDGETYAVSGGLHGVGVSVVNALSTRLEATVLRDGYEWFQYYDRSVPGKLKQGGETKETGTTIRFWADPEIFETTDYNFETVARRLQEMAFLNKGLTIELTDERVTAEEVVDDVVKDTAEAPKTADEKAAEATGPSKVKHRVFHYPGGLVDYVKHINRTKTPIQQSIIDFDGKGPGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGF... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:12000834}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; Note=Binds two Mg(2+) per subunit. The... | DNA topological change [GO:0006265]; DNA-templated DNA replication [GO:0006261] | chromosome [GO:0005694]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA negative supercoiling activity [GO:0034335]; metal ion binding [GO:0046872] | PF00204;PF00986;PF02518;PF01751; | 3.30.230.10;3.40.50.670;3.30.565.10; | Type II topoisomerase GyrB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:12000834}. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01898, ECO:0000269|PubMed:12000834}; | null | null | null | null | FUNCTION: Supercoils relaxed DNA in an ATP-dependent manner (PubMed:8574396). A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, also catalyzes the interconversion of other topol... | Mycolicibacterium smegmatis (Mycobacterium smegmatis) |
P0C565 | CHRYS_TANCI | MACSSSLSSKWASWGASSRPHPSVQPFVTRKNVVRYHKPTSELSYSPLTTTLSSNLDSQFMQVYETLKSELIHDPSFEFDDDSRQWVERMIDYNVPGGKMVRGYSVVDSYQLLKGEELTEDEAFLACALGWCTEWLQAFILVLDDIMDGSHTRRGQPCWFRLPEVGVVAINDGVLLRNHVHRILKKYFQGKPYYVHLLDLFNETEFQTISGQMIDTICRLAGQKDLSKYTMTLNRRIVQYKGSYYSCYLPIACALLMFGENLEDHVQVKDILVELGMYYQIQNDYLDTFGDPDVFGKTGTDIEECKCSWLIAKALELANE... | 2.5.1.67; 3.7.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11287653}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:11287653}; | farnesyl diphosphate biosynthetic process [GO:0045337]; isoprenoid biosynthetic process [GO:0008299] | chloroplast [GO:0009507] | chrysanthemyl diphosphate synthase activity [GO:0033849]; dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:25378387}. | CATALYTIC ACTIVITY: Reaction=2 dimethylallyl diphosphate = (R,R)-chrysanthemyl diphosphate + diphosphate; Xref=Rhea:RHEA:14009, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58819; EC=2.5.1.67; Evidence={ECO:0000269|PubMed:11287653, ECO:0000269|PubMed:25378387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=600 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:11287653}; KM=196 uM for chrysanthemyl diphosphate {ECO:0000269|PubMed:25378387}; Note=kcat is 0.5 min(-1) with dimethylallyl diphosphate as substrate (PubMed:11287653). kcat is 0.0033 min(-1) with chrysanthe... | PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:25378387}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-8. {ECO:0000269|PubMed:11287653}; | null | FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide (PubMed:30468448). Catalyzes the condensation of two molecules of dimethylallyl diphosphate to produce chrysanthemyl diphosphate (CPP), a monoterpene with a non-head-to-tail or irregular c1'-2-3 linkage ... | Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium) |
P0C573 | HBEAG_HBVD3 | MQLFHLCLIISCSCPTVQASKLCLGWLWGMDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGVNLEDPASRDLVVSYVNTNMGLKFRQLLWFHISCLTFGRETVIEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; T=4 icosahedral viral capsid [GO:0039619] | DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF08290;PF00906; | 1.10.4090.10; | Orthohepadnavirus precore antigen family | PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04076}.; PTM: Cleaved by host furin. {ECO:0000255|HAMAP-Rule:MF_04076}. | SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_04076}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04076}. | null | null | null | null | null | FUNCTION: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury duri... | Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) |
P0C577 | VSPG_BITGA | VVGGAECKIDGHRCLALLY | 3.4.21.55 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type peptidase activity [GO:0008236]; toxin activity [GO:0090729] | null | null | Peptidase S1 family, Snake venom subfamily | PTM: Glycosylated.; PTM: Contains five disulfide bonds. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.55; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for Tosyl-L-arginine methyl ester (TAME) {ECO:0000269|PubMed:3522580}; KM=0.13 mM for Tosyl-Gly-Pro-Arg 4-nitroanilide {ECO:0000269|PubMed:3522580}; KM=0.82 mM for H-D-Pro-hexahydrotyrosyl-Arg 4-nitroanilide {ECO:0000269|PubMed:3522580}; KM=0.88 mM for H-D-... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius with tosyl-Arg-methyl ester (TAME) as substrate and 37 degrees Celsius with natural substrates. {ECO:0000269|PubMed:3522580}; | FUNCTION: Thrombin-like snake venom serine protease. Releases both fibrinopeptides A and B from fibrinogen (FGA and FGB) to form fibrin clots. Also activates factor XIII (F13A). The activity of the enzyme is stabilized by calcium ion. | Bitis gabonica (Gaboon adder) (Gaboon viper) |
P0C581 | PAN2_NEUCR | MDSRDWTQLGCVAYPSPIHPDYHAGPASTIAFDNQDELLWIGTQKGFAGSFIGRELKRFTAFRIHPETDGPLRQFLFVDKGVIFLGSRSVYMAARSGVPIWSIRHESMQDLRAMSFTSKGTSEILVAGWQNKMLVIDVNKGEVVKELPTQDQYSFLKMSRYICAATNKGTVNILDPITFTIKKQWQAHGAFINDLDTSNDFIVTCGGSHRQTHNTPAILDPYVKVFDLKNMSAMNPVPFAPLAAHVRMHPRMLTTAIVVNQAGQIHVTDLLNPSNSQVCYTQPQGVVLHFDVSRTGEGKALADNKHNTYVWGSPNKIQFT... | 3.1.13.4 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182}; | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289] | P-body [GO:0000932]; PAN complex [GO:0031251] | metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; poly(A)-specific ribonuclease activity [GO:0004535] | PF20770;PF00929;PF13423; | 3.90.70.10;3.30.420.10;2.130.10.10; | Peptidase C19 family, PAN2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; | null | null | null | null | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pabp-1. PAN deadenylation is followed by rapid degradation of the ... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P0C586 | SSY23_ORYSI | MSSAVVASSTTFLVALASSASRGGPRRGRVVGVAAPPALLYDGRAGRLALRAPPPPRPRPRRRDAGVVRRADDGENEAAVERAGEDDEEEEEFSSGAWQPPRSRRGGVGKVLKRRGTVPPVGRYGSGGDAARVRGAAAPAPAPTQDAASSKNGALLSGRDDDTPASRNGSVVTGADKPAAATPPVTITKLPAPDSPVILPSVDKPQPEFVIPDATAPAPPPPGSNPRSSAPLPKPDNSEFAEDKSAKVVESAPKPKATRSSPIPAVEEETWDFKKYFDLNEPDAAEDGDDDDDWADSDASDSEIDQDDDSGPLAGENVMN... | 2.4.1.21 | null | starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507] | alpha-1,4-glucan synthase activity [GO:0033201]; glycogen (starch) synthase activity [GO:0004373]; starch synthase activity [GO:0009011] | PF13692;PF08323; | 3.40.50.2000; | Glycosyltransferase 1 family, Bacterial/plant glycogen synthase subfamily | null | SUBCELLULAR LOCATION: Plastid, amyloplast. Plastid, chloroplast. Note=Amyloplast or chloroplast, granule-bound and soluble. | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: Plays an important role during endosperm starch synthesis. Determines the type of amylopectin structure of starch grain. Synthesizes long B1 amylopectin chains by elongating short A and B1 chains, independently of the other soluble starch synthases. Barely active in japonica subspecies. {ECO:0000269|PubMed:14... | Oryza sativa subsp. indica (Rice) |
P0C588 | CNNM4_RAT | MAPGGGGGRRDGWPARGRLLLAALLLLLWTRAASGQSSPQQSVILGMRLASCNKSCGMNPDGIIFVSEGSTVNLRLYGHRLGEISSNLISFTEVDDAETVHNSTNCLELTKDLVVQRLVNVSRGNTSGMLVVITKFLRRSENMKLYALCTRTRADGPWLKWTDKDSLLFMVEEHGRFLPLWLHILLVLVLLVLSGIFSGLNLGLMALDPMELRIVQNCGTEKERRYARKIEPIRRKGNYLLCSLLLGNVLVNTSLTILLDNLIGSGIMAVASSTIGIVIFGEILPQALCSRHGLAVGANTIVLTKIFMLLTFPLSFPISK... | null | null | enamel mineralization [GO:0070166]; intracellular manganese ion homeostasis [GO:0030026]; intracellular monoatomic cation homeostasis [GO:0030003]; magnesium ion homeostasis [GO:0010960]; magnesium ion transport [GO:0015693]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | magnesium ion transmembrane transporter activity [GO:0015095]; sodium ion transmembrane transporter activity [GO:0015081] | PF00571;PF01595; | 3.10.580.10;2.60.120.10; | ACDP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15840172}; Multi-pass membrane protein {ECO:0000305|PubMed:15840172}. | null | null | null | null | null | FUNCTION: Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions. May play a role in biomineralization and retinal function. {ECO:0000269|PubMed:15840172, ECO:0000269|PubMed:19200525}. | Rattus norvegicus (Rat) |
P0C5A3 | DPNP_ORYSA | MSQAAGNPYAAELAAAKKAVTLAARLCQAVQKDILQSGVQSKADQSPVTVADYGSQILVSLVLKMEAPASSSFSMVAEEDSEELRKEGAEEILENITELVNETIVDDGTYSIYFSKEGILSAIDDGKSEGGPSGRHWVLDPIDGTKGFLRGDQYAIALALLDEGKVVLGVLACPNLSLGSIGNLNGGSSGDQVGALFSATIGCGAEVESLQGSPAQKISVCSIDNPVEASFFESYEGAHSLRDLTGSIAEKLGVQAPPVRIDSQAKYGALARGDGAIYLRFPHKGYREKIWDHAAGSIVVTEAGGLVTDASGNDLDFSKG... | 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7493934}; | phosphatidylinositol phosphate biosynthetic process [GO:0046854]; sulfate assimilation [GO:0000103] | null | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; metal ion binding [GO:0046872] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | null | null | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:7493934}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for 3'-phosphoadenylyl sulfate {ECO:0000269|PubMed:7493934}; KM=240 uM for adenosine 3',5'-bisphosphate {ECO:0000269|PubMed:7493934}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:7493934}; | null | FUNCTION: Phosphatase that converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Shows no activity on myo-inositol 1-phosphate, beta-... | Oryza sativa (Rice) |
P0C5B4 | VSPGL_GLOSH | MVLIRVQANLLILQLSYAQKSSELIIGGDECNINEHRFLVALYTSRSRRFYCGGTLINQEWVLTAAHCDRKNIRIKLGMHSEKVPNEDAETRVPKEKFFCLSSKTYTKWDKDIMLMRLKRPVNNSTHIAPVSLPSNPPSVDSVCRVMGWGTITSPQETYPDVPHCANINILDYEVCQAAHGGLPATSRTLCAGILKGGKDSCKGDSGGPLICNGQFQGIASWGAHPCGQSLKPGVYTKVFDYTEWIQSIIAGNTDATCPP | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}; | FUNCTION: Thrombin-like snake venom serine protease. The recombinant form clots fibrinogen by cleaving fibrinogen Aalpha chain (FGA), and slowly Bbeta chain (FGB). Has amidolytic activities. {ECO:0000269|PubMed:19286459, ECO:0000269|PubMed:19639313}. | Gloydius shedaoensis (Shedao island pit viper) (Agkistrodon shedaoensis) |
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